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Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations.

Abstract:

Using a data base of 85 high resolution protein crystal structures the distributions of main chain torsion angles, both in secondary structure and in coil regions where no secondary structure is present, have been analysed. These torsion angle distributions have been used to predict NMR homonuclear and heteronuclear coupling constants for residues in secondary structure using known Karplus relationships. For alpha helices, 3(10) helices and beta strands mean predicted 3JHN alpha coupling cons...

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Publication status:
Published

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Publisher copy:
10.1006/jmbi.1996.0041

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Role:
Author
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Journal:
Journal of molecular biology
Volume:
255
Issue:
3
Pages:
494-506
Publication date:
1996-01-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:ede6072f-646f-4bf1-972e-2afedef01ab7
Source identifiers:
35897
Local pid:
pubs:35897

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